Bradykinin B2 and dopamine D2 receptors form a functional dimer
| Autor: | Monika Piwowar, Magdalena Tworzydło, Ibeth Guevara-Lora, Anna Niewiarowska-Sendo, Agnieszka Polit, Andrzej Kozik |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Receptor Bradykinin B2 Protein Conformation bradykinin 2 receptor D1-like receptor Immune receptor Bradykinin Rhodopsin-like receptors 03 medical and health sciences 0302 clinical medicine cAMP-dependent signaling Humans Bradykinin receptor Receptor Molecular Biology G protein-coupled receptor heterodimerization Chemistry Receptors Dopamine D2 Ca^{2+}-dependent signaling dopamine 2 receptor Cell Biology Cell biology 030104 developmental biology HEK293 Cells Biochemistry Dopamine receptor D2-like receptor Dimerization 030217 neurology & neurosurgery Signal Transduction |
| Zdroj: | Biochimica et biophysica acta. Molecular cell research. 1864(10) |
| ISSN: | 0167-4889 |
| Popis: | In recent years a wide range of studies have shown that G protein-coupled receptors modulate a variety of cell functions through the formation of dimers. For instance, there is growing evidence for the dimerization of bradykinin or dopamine receptors, both as homodimers and heterodimers. A discovery of direct interactions of angiotensin II receptors with bradykinin 2 receptor (B2R) or dopamine D2 (D2R) receptor has led to a hypothesis on a potential dimerization between two latter receptors. In this study, we have demonstrated a constitutive colocalization of receptors on the membranes of HEK293 cells transiently transfected with plasmid vectors encoding B2R and D2R, fused with fluorescent proteins. The receptor colocalization was significantly enhanced by specific agonists of B2R or D2R after 5min following the addition, whereas simultaneous stimulation with these agonists did not influence the B2R/D2R colocalization level. In addition, B2R-D2R heterodimerization was confirmed with FLIM-FRET technique. The most characteristic signaling pathways for B2R and D2R, dependent on intracellular Ca2+ and cAMP concentration, respectively, were analyzed in cells presenting similar endogenous expression of B2R and D2R. Significant changes in receptors' signaling were observed after simultaneous stimulation with agonists, suggesting transformations in proteins' conformation after dimerization. The evidence of B2R-D2R dimerization may open new perspectives in the modulation of diverse cellular functions which depend on their activation. |
| Databáze: | OpenAIRE |
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